SitesBLAST
Comparing AO356_24890 FitnessBrowser__pseudo5_N2C3_1:AO356_24890 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P47229 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; HOPDA hydrolase; 2,6-dioxo-6-phenylhexa-3-enoate hydrolase; EC 3.7.1.8 from Paraburkholderia xenovorans (strain LB400) (see paper)
30% identity, 66% coverage: 123:367/370 of query aligns to 25:283/286 of P47229
- S112 (= S206) mutation to A: Catalyzes the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-265.
- H265 (= H349) mutation to A: Unable to catalyze the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-112.
2og1A Crystal structure of bphd, a c-c hydrolase from burkholderia xenovorans lb400 (see paper)
30% identity, 66% coverage: 123:367/370 of query aligns to 24:282/285 of 2og1A
- active site: G41 (≠ F141), G42 (= G142), G44 (≠ D144), N110 (≠ H205), S111 (= S206), M112 (= M207), L155 (= L243), R189 (= R282), A207 (≠ D300), D236 (= D326), H264 (= H349), W265 (≠ M350)
- binding glycerol: Y52 (≠ H152), E184 (≠ Q272)
P77044 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase; 2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; EC 3.7.1.14 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 69% coverage: 115:369/370 of query aligns to 16:287/288 of P77044
- S44 (≠ F141) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (≠ H205) mutation to A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity.; mutation to H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- S114 (= S206) Transition state stabilizer; mutation to A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.; mutation to G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.
- H118 (≠ A210) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (≠ E267) mutation to D: 100-fold decrease in catalytic activity.; mutation to G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively.
- R192 (= R282) Catalytic role in ketonization of the dienol substrate (substrate destabilization); mutation to K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively.; mutation to Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively.
- C265 (≠ Q347) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H349) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (≠ M350) mutation to G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2rhwA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3,10-di-fluoro hopda (see paper)
29% identity, 66% coverage: 123:367/370 of query aligns to 22:280/283 of 2rhwA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding 3-fluoro-6-(4-fluorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (vs. gap), F172 (≠ L262), L210 (≠ V305), F236 (≠ I328), V237 (≠ I329), H262 (= H349)
2rhtA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3-cl hopda (see paper)
29% identity, 66% coverage: 123:367/370 of query aligns to 22:280/283 of 2rhtA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), I150 (vs. gap), L153 (= L243), F172 (≠ L262), R187 (= R282), F236 (≠ I328), V237 (≠ I329), H262 (= H349)
2puhA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
29% identity, 66% coverage: 123:367/370 of query aligns to 22:280/283 of 2puhA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G140), G39 (≠ F141), G40 (= G142), N108 (≠ H205), A109 (≠ S206), M110 (= M207), I150 (vs. gap), F172 (≠ L262), R187 (= R282), L210 (≠ V305), W213 (≠ R308), V237 (≠ I329), H262 (= H349), W263 (≠ M350)
P9WNH5 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase; 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; HOPDA hydrolase; Meta-cleavage product hydrolase; MCP hydrolase; EC 3.7.1.17; EC 3.7.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 17:287/291 of P9WNH5
- S114 (= S206) mutation to A: Reduces the hydrolase activity.
2pujA Crystal structure of the s112a/h265a double mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
29% identity, 66% coverage: 123:367/370 of query aligns to 22:280/283 of 2pujA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), A262 (≠ H349), W263 (≠ M350)
- binding (2e,4e)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (vs. gap), L153 (= L243), F172 (≠ L262), R187 (= R282), V237 (≠ I329)
5jzbA Crystal structure of hsad bound to 3,5-dichlorobenzene sulphonamide (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/282 of 5jzbA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), S108 (= S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding 3,5-dichlorobenzene-1-sulfonamide: G39 (≠ F141), G40 (= G142), S108 (= S206), L109 (≠ M207), G134 (≠ A232), L152 (= L243), N238 (≠ I329)
7zm4A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc31 (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 7zm4A
7zm3A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc17 (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 7zm3A
7zm2A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc8b (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 7zm2A
7zm1A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc7b (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 7zm1A
5jzsB Hsad bound to 3,5-dichloro-4-hydroxybenzoic acid (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 5jzsB
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), S108 (= S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding 3,5-dichloro-4-hydroxybenzoic acid: G39 (≠ F141), S108 (= S206), G148 (vs. gap), V149 (vs. gap), L152 (= L243), V237 (≠ I328)
5jz9A Crystal structure of hsad bound to 3,5-dichloro-4- hydroxybenzenesulphonic acid (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/284 of 5jz9A
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), S108 (= S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding 3,5-dichloro-4-hydroxybenzene-1-sulfonic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), S108 (= S206), G148 (vs. gap), L152 (= L243), F167 (≠ P258), M171 (≠ L262), V237 (≠ I328), H263 (= H349), W264 (≠ M350)
Q8R2Y0 Monoacylglycerol lipase ABHD6; 2-arachidonoylglycerol hydrolase; Abhydrolase domain-containing protein 6; EC 3.1.1.23 from Mus musculus (Mouse) (see paper)
28% identity, 66% coverage: 125:368/370 of query aligns to 62:325/336 of Q8R2Y0
- S148 (= S206) mutation to A: Loss of the lipid hydrolase activity.
6i8wB Crystal structure of a membrane phospholipase a, a novel bacterial virulence factor (see paper)
28% identity, 70% coverage: 109:367/370 of query aligns to 38:304/310 of 6i8wB
Sites not aligning to the query:
2wugA Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopda (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/283 of 2wugA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), A108 (≠ S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G140), G39 (≠ F141), G40 (= G142), A108 (≠ S206), L109 (≠ M207), M202 (≠ L293), H263 (= H349), W264 (≠ M350)
2wufB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with 4,9dsha (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/282 of 2wufB
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), A108 (≠ S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding (3e,5r)-8-[(1s,3ar,4r,7as)-1-hydroxy-7a-methyl-5-oxooctahydro-1h-inden-4-yl]-5-methyl-2,6-dioxooct-3-enoate: G38 (= G140), G39 (≠ F141), G40 (= G142), A108 (≠ S206), L109 (≠ M207), L152 (= L243), F206 (≠ L297), H263 (= H349), W264 (≠ M350)
2wueB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopoda (see paper)
29% identity, 68% coverage: 115:367/370 of query aligns to 11:281/282 of 2wueB
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N107 (≠ H205), A108 (≠ S206), L109 (≠ M207), R186 (≠ M277), D235 (= D326), H263 (= H349), W264 (≠ M350)
- binding (3e,5r)-8-(2-chlorophenyl)-5-methyl-2,6-dioxooct-3-enoate: G38 (= G140), G39 (≠ F141), G40 (= G142), A108 (≠ S206), L109 (≠ M207), V149 (vs. gap), L152 (= L243), M202 (≠ L293), F206 (≠ L297), V237 (≠ I328), H263 (= H349)
Query Sequence
>AO356_24890 FitnessBrowser__pseudo5_N2C3_1:AO356_24890
MSQIHTLTMPKWGLSMTEGRVDAWLKEEGQAITKGDEVMDVETDKISSSVEAPFSGILRR
QVARQDETLAVGALLGIVVDGEASDAEIDAVIEQFQSNFVPGDSADEDSGPTPQKVELDG
RVIRYFERGEGGTPLVLVHGFGGDLNNWLFNHEALAVGRRVIALDLPGHGESSKTLQRGD
LDELSGVVLALLDHLDINAVHLVGHSMGGAVSLNAARLMPQRVRSLTLIGSAGLGAQING
GYLQGFVEAANRNALKPPLVQLFSNAELVTRQMLDDMLKYKRLEGVDAALRQLSATLFAD
GRQQVDLREVVQAGHVPTLVIWGSDDAIIPAAHGEGLAAQVEVLPGQGHMVQMEAAEQVN
RSILEFIAQH
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory